Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 13 to 24 of 476 entries
Sorted by: Best Match Show Resources per page
Polarizable Force Field for Protein with Charge Response Kernel.

Journal of chemical theory and computation

Isegawa M, Kato S.
PMID: 26631793
J Chem Theory Comput. 2009 Oct 13;5(10):2809-21. doi: 10.1021/ct900295u. Epub 2009 Sep 24.

We present a molecular mechanical force field for polypeptides and proteins involving the electronic polarization effect described with the charge response kernel. All of the electrostatic parameters for 20 amino acids are obtained by ab initio electronic structure calculations...

Cite
Isegawa M, Kato S. Polarizable Force Field for Protein with Charge Response Kernel. J Chem Theory Comput. 2009;5(10):2809-21doi: 10.1021/ct900295u.
Isegawa, M., & Kato, S. (2009). Polarizable Force Field for Protein with Charge Response Kernel. Journal of chemical theory and computation, 5(10), 2809-21. https://doi.org/10.1021/ct900295u
Isegawa, Miho, and Kato, Shigeki. "Polarizable Force Field for Protein with Charge Response Kernel." Journal of chemical theory and computation vol. 5,10 (2009): 2809-21. doi: https://doi.org/10.1021/ct900295u
Isegawa M, Kato S. Polarizable Force Field for Protein with Charge Response Kernel. J Chem Theory Comput. 2009 Oct 13;5(10):2809-21. doi: 10.1021/ct900295u. Epub 2009 Sep 24. PMID: 26631793.
Copy Download .nbib Format: NLM
Application of Reductive Samariation to the Synthesis of Small Unnatural Peptides.

Angewandte Chemie (International ed. in English)

Ricci M, Madariaga L, Skrydstrup T.
PMID: 10649389
Angew Chem Int Ed Engl. 2000 Jan;39(1):242-246. doi: 10.1002/(sici)1521-3773(20000103)39:1<242::aid-anie242>3.0.co;2-r.

Considering that the amide NH groups are neither protected nor deprotonated, reductive samariation in the presence of a carbonyl substrate is a remarkably efficient method for the formation of a C-C bond. This was shown for a series of...

Cite
Ricci M, Madariaga L, Skrydstrup T. Application of Reductive Samariation to the Synthesis of Small Unnatural Peptides. Angew Chem Int Ed Engl. 2000;39(1):242-246doi: 10.1002/(sici)1521-3773(20000103)39:1<242::aid-anie242>3.0.co;2-r.
Ricci, M., Madariaga, L., & Skrydstrup, T. (2000). Application of Reductive Samariation to the Synthesis of Small Unnatural Peptides. Angewandte Chemie (International ed. in English), 39(1), 242-246. https://doi.org/10.1002/(sici)1521-3773(20000103)39:1<242::aid-anie242>3.0.co;2-r
Ricci, et al. "Application of Reductive Samariation to the Synthesis of Small Unnatural Peptides." Angewandte Chemie (International ed. in English) vol. 39,1 (2000): 242-246. doi: https://doi.org/10.1002/(sici)1521-3773(20000103)39:1<242::aid-anie242>3.0.co;2-r
Ricci M, Madariaga L, Skrydstrup T. Application of Reductive Samariation to the Synthesis of Small Unnatural Peptides. Angew Chem Int Ed Engl. 2000 Jan;39(1):242-246. doi: 10.1002/(sici)1521-3773(20000103)39:1<242::aid-anie242>3.0.co;2-r. PMID: 10649389.
Copy Download .nbib Format: NLM
Di-tert-butyl Dicarbonate: A Novel Reagent for the Efficient Synthesis of Dipeptides under Mild Conditions.

The Journal of organic chemistry

Mohapatra DK, Datta A.
PMID: 11674699
J Org Chem. 1999 Sep 03;64(18):6879-6880. doi: 10.1021/jo982229r.

No abstract available.

Cite
Mohapatra DK, Datta A. Di-tert-butyl Dicarbonate: A Novel Reagent for the Efficient Synthesis of Dipeptides under Mild Conditions. J Org Chem. 1999;64(18):6879-6880doi: 10.1021/jo982229r.
Mohapatra, D. K., & Datta, A. (1999). Di-tert-butyl Dicarbonate: A Novel Reagent for the Efficient Synthesis of Dipeptides under Mild Conditions. The Journal of organic chemistry, 64(18), 6879-6880. https://doi.org/10.1021/jo982229r
Mohapatra, Debendra K., and Datta, Apurba. "Di-tert-butyl Dicarbonate: A Novel Reagent for the Efficient Synthesis of Dipeptides under Mild Conditions." The Journal of organic chemistry vol. 64,18 (1999): 6879-6880. doi: https://doi.org/10.1021/jo982229r
Mohapatra DK, Datta A. Di-tert-butyl Dicarbonate: A Novel Reagent for the Efficient Synthesis of Dipeptides under Mild Conditions. J Org Chem. 1999 Sep 03;64(18):6879-6880. doi: 10.1021/jo982229r. PMID: 11674699.
Copy Download .nbib Format: NLM
Use of Steric Interactions To Control Peptide Turn Geometry. Synthesis of Type VI beta-Turn Mimics with 5-tert-Butylproline.

The Journal of organic chemistry

Halab L, Lubell WD.
PMID: 11674436
J Org Chem. 1999 Apr 30;64(9):3312-3321. doi: 10.1021/jo990294a.

The influences of steric interactions on peptide geometry were studied to develop a novel means for generating type VIa beta-turn mimics. (2S,5R)-5-tert-Butylproline and L-proline were respectively introduced at the C-terminal residue of N-(acetyl)dipeptide N'-methylamides 1 and 2. The relative...

Cite
Halab L, Lubell WD. Use of Steric Interactions To Control Peptide Turn Geometry. Synthesis of Type VI beta-Turn Mimics with 5-tert-Butylproline. J Org Chem. 1999;64(9):3312-3321doi: 10.1021/jo990294a.
Halab, L., & Lubell, W. D. (1999). Use of Steric Interactions To Control Peptide Turn Geometry. Synthesis of Type VI beta-Turn Mimics with 5-tert-Butylproline. The Journal of organic chemistry, 64(9), 3312-3321. https://doi.org/10.1021/jo990294a
Halab, Liliane, and Lubell, William D.. "Use of Steric Interactions To Control Peptide Turn Geometry. Synthesis of Type VI beta-Turn Mimics with 5-tert-Butylproline." The Journal of organic chemistry vol. 64,9 (1999): 3312-3321. doi: https://doi.org/10.1021/jo990294a
Halab L, Lubell WD. Use of Steric Interactions To Control Peptide Turn Geometry. Synthesis of Type VI beta-Turn Mimics with 5-tert-Butylproline. J Org Chem. 1999 Apr 30;64(9):3312-3321. doi: 10.1021/jo990294a. PMID: 11674436.
Copy Download .nbib Format: NLM
Purification and characterization of a novel dipeptidase from carp ordinary muscle.

Journal of marine biotechnology

Aranishi F, Watanabe T, Osatomi K, Cao M, Hara K, Ishihara T.
PMID: 9701633
J Mar Biotechnol. 1998 Aug;6(3):129-35.

A novel dipeptidase was purified to homogeneity from the crude extract of carp ordinary muscle with an increase in specific activity of 4041-fold and a 4% recovery rate. The enzyme was determined to have molecular weights of 54,000 after...

Cite
Aranishi F, Watanabe T, Osatomi K, et al. Purification and characterization of a novel dipeptidase from carp ordinary muscle. J Mar Biotechnol. 1998;6(3):129-35
Aranishi, F., Watanabe, T., Osatomi, K., Cao, M., Hara, K., & Ishihara, T. (1998). Purification and characterization of a novel dipeptidase from carp ordinary muscle. Journal of marine biotechnology, 6(3), 129-35.
Aranishi, et al. "Purification and characterization of a novel dipeptidase from carp ordinary muscle." Journal of marine biotechnology vol. 6,3 (1998): 129-35.
Aranishi F, Watanabe T, Osatomi K, Cao M, Hara K, Ishihara T. Purification and characterization of a novel dipeptidase from carp ordinary muscle. J Mar Biotechnol. 1998 Aug;6(3):129-35. PMID: 9701633.
Copy Download .nbib Format: NLM
Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine.

Journal of marine biotechnology

Aranishi F, Watanabe T, Osatomi K, Cao M, Hara K, Ishihara T.
PMID: 9701637
J Mar Biotechnol. 1998 Aug;6(3):157-62.

Although carp muscular and intestinal dipeptidases are metalloenzymes acting only on dipeptides, some structural and enzymatic differences occur between them. The present study verifies distinctive actions during dipeptide hydrolysis by these enzymes in terms of their kinetic characterization. The...

Cite
Aranishi F, Watanabe T, Osatomi K, et al. Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine. J Mar Biotechnol. 1998;6(3):157-62
Aranishi, F., Watanabe, T., Osatomi, K., Cao, M., Hara, K., & Ishihara, T. (1998). Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine. Journal of marine biotechnology, 6(3), 157-62.
Aranishi, et al. "Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine." Journal of marine biotechnology vol. 6,3 (1998): 157-62.
Aranishi F, Watanabe T, Osatomi K, Cao M, Hara K, Ishihara T. Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine. J Mar Biotechnol. 1998 Aug;6(3):157-62. PMID: 9701637.
Copy Download .nbib Format: NLM
Transepithelial Transport and Metabolism of Boronated Dipeptides Across Caco-2 and HCT-8 Cell Monolayers.

Metal-based drugs

Elkins AL, Eley JG, Miller Iii MC, Hall IH, Sood A, Spielvogel B.
PMID: 18475758
Met Based Drugs. 1996;3(6):277-86. doi: 10.1155/MBD.1996.277.

Oral delivery of proteins and peptides as therapeutic agents is problematic due to their low bioavailability. This study examined the effect of boronation on the transepithelial transport and metabolism of three glycine-phenylalanine dipeptides in Caco-2 and HCT-8 cell monolayers....

Cite
Elkins AL, Eley JG, Miller Iii MC, et al. Transepithelial Transport and Metabolism of Boronated Dipeptides Across Caco-2 and HCT-8 Cell Monolayers. Met Based Drugs. 1996;3(6):277-86doi: 10.1155/MBD.1996.277.
Elkins, A. L., Eley, J. G., Miller Iii, M. C., Hall, I. H., Sood, A., & Spielvogel, B. (1996). Transepithelial Transport and Metabolism of Boronated Dipeptides Across Caco-2 and HCT-8 Cell Monolayers. Metal-based drugs, 3(6), 277-86. https://doi.org/10.1155/MBD.1996.277
Elkins, A L, et al. "Transepithelial Transport and Metabolism of Boronated Dipeptides Across Caco-2 and HCT-8 Cell Monolayers." Metal-based drugs vol. 3,6 (1996): 277-86. doi: https://doi.org/10.1155/MBD.1996.277
Elkins AL, Eley JG, Miller Iii MC, Hall IH, Sood A, Spielvogel B. Transepithelial Transport and Metabolism of Boronated Dipeptides Across Caco-2 and HCT-8 Cell Monolayers. Met Based Drugs. 1996;3(6):277-86. doi: 10.1155/MBD.1996.277. PMID: 18475758; PMCID: PMC2365028.
Copy Download .nbib Format: NLM
Diketopiperazine formation during investigations of amino Acid racemization in dipeptides.

Science (New York, N.Y.)

Steinberg S, Bada JL.
PMID: 17794841
Science. 1981 Jul 31;213(4507):544-5. doi: 10.1126/science.213.4507.544.

The formation of diketopiperazines from the dipeptides isoleucylglycine and glycylisoleucine was investigated at 132 degrees C over the pH range approximately 2 to 10. At pH 6.2, approximately 50 percent of the original dipeptides were converted to the diketopiperazines...

Cite
Steinberg S, Bada JL. Diketopiperazine formation during investigations of amino Acid racemization in dipeptides. Science. 1981;213(4507):544-5doi: 10.1126/science.213.4507.544.
Steinberg, S., & Bada, J. L. (1981). Diketopiperazine formation during investigations of amino Acid racemization in dipeptides. Science (New York, N.Y.), 213(4507), 544-5. https://doi.org/10.1126/science.213.4507.544
Steinberg, S, and Bada, J L. "Diketopiperazine formation during investigations of amino Acid racemization in dipeptides." Science (New York, N.Y.) vol. 213,4507 (1981): 544-5. doi: https://doi.org/10.1126/science.213.4507.544
Steinberg S, Bada JL. Diketopiperazine formation during investigations of amino Acid racemization in dipeptides. Science. 1981 Jul 31;213(4507):544-5. doi: 10.1126/science.213.4507.544. PMID: 17794841.
Copy Download .nbib Format: NLM
Amide I vibrational circular dichroism of polypeptides: generalized fragmentation approximation method.

The Journal of chemical physics

Choi JH, Kim JS, Cho M.
PMID: 15910065
J Chem Phys. 2005 May 01;122(17):174903. doi: 10.1063/1.1888390.

Fragment analyses of vibrational circular dichroic response of dipeptides were carried out recently [Choi and Cho, J. Chem. Phys. 120, 4383 (2004)]. In the present paper, by using a minimal size unit peptide containing two chiral carbons covalently bonded...

Cite
Choi JH, Kim JS, Cho M. Amide I vibrational circular dichroism of polypeptides: generalized fragmentation approximation method. J Chem Phys. 2005;122(17):174903doi: 10.1063/1.1888390.
Choi, J. H., Kim, J. S., & Cho, M. (2005). Amide I vibrational circular dichroism of polypeptides: generalized fragmentation approximation method. The Journal of chemical physics, 122(17), 174903. https://doi.org/10.1063/1.1888390
Choi, Jun-Ho, et al. "Amide I vibrational circular dichroism of polypeptides: generalized fragmentation approximation method." The Journal of chemical physics vol. 122,17 (2005): 174903. doi: https://doi.org/10.1063/1.1888390
Choi JH, Kim JS, Cho M. Amide I vibrational circular dichroism of polypeptides: generalized fragmentation approximation method. J Chem Phys. 2005 May 01;122(17):174903. doi: 10.1063/1.1888390. PMID: 15910065.
Copy Download .nbib Format: NLM
Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.).

Plant physiology

Waters SP, Dalling MJ.
PMID: 16663327
Plant Physiol. 1983 Dec;73(4):1048-54. doi: 10.1104/pp.73.4.1048.

Iminopeptidase (EC 3.4.11.5) was substantially purified from the primary leaves of 7-day-old wheat seedlings (Triticum aestivum L.). The purification procedure consisted of five steps: acid precipitation, molecular exclusion chromatography on Sephacryl S-200, Ultrogel AcA 44, Sepharose 2B and ion-exchange...

Cite
Waters SP, Dalling MJ. Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.). Plant Physiol. 1983;73(4):1048-54doi: 10.1104/pp.73.4.1048.
Waters, S. P., & Dalling, M. J. (1983). Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.). Plant physiology, 73(4), 1048-54. https://doi.org/10.1104/pp.73.4.1048
Waters, S P, and Dalling, M J. "Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.)." Plant physiology vol. 73,4 (1983): 1048-54. doi: https://doi.org/10.1104/pp.73.4.1048
Waters SP, Dalling MJ. Purification and Characterization of an Iminopeptidase from the Primary Leaf of Wheat (Triticum aestivum L.). Plant Physiol. 1983 Dec;73(4):1048-54. doi: 10.1104/pp.73.4.1048. PMID: 16663327; PMCID: PMC1066605.
Copy Download .nbib Format: NLM
Separation and determination of l-tyrosine and its metabolites by capillary zone electrophoresis with a wall-jet amperometric detection.

Talanta

Huang Y, Jiang X, Wang W, Duan J, Chen G.
PMID: 18970894
Talanta. 2006 Dec 15;70(5):1157-63. doi: 10.1016/j.talanta.2006.03.009. Epub 2006 Jun 14.

A method of capillary electrophoresis with wall-jet amperometric detection (AD) has been developed for separation and determination of l-tyrosine (Tyr) and its metabolites, such as Tyramine (TA), p-hydroxyphenylpyruvic (pHPP), homogentisic acid (HGA) and some dipeptides containing Tyr, such as...

Cite
Huang Y, Jiang X, Wang W, et al. Separation and determination of l-tyrosine and its metabolites by capillary zone electrophoresis with a wall-jet amperometric detection. Talanta. 2006;70(5):1157-63doi: 10.1016/j.talanta.2006.03.009.
Huang, Y., Jiang, X., Wang, W., Duan, J., & Chen, G. (2006). Separation and determination of l-tyrosine and its metabolites by capillary zone electrophoresis with a wall-jet amperometric detection. Talanta, 70(5), 1157-63. https://doi.org/10.1016/j.talanta.2006.03.009
Huang, Ying, et al. "Separation and determination of l-tyrosine and its metabolites by capillary zone electrophoresis with a wall-jet amperometric detection." Talanta vol. 70,5 (2006): 1157-63. doi: https://doi.org/10.1016/j.talanta.2006.03.009
Huang Y, Jiang X, Wang W, Duan J, Chen G. Separation and determination of l-tyrosine and its metabolites by capillary zone electrophoresis with a wall-jet amperometric detection. Talanta. 2006 Dec 15;70(5):1157-63. doi: 10.1016/j.talanta.2006.03.009. Epub 2006 Jun 14. PMID: 18970894.
Copy Download .nbib Format: NLM
Enrichment techniques and trace analysis with microbore columns in liquid chromatography.

Journal of pharmaceutical and biomedical analysis

Krejci M, Slais K, Kourilová D, Vespalcová M.
PMID: 16867748
J Pharm Biomed Anal. 1984;2(2):197-205. doi: 10.1016/0731-7085(84)80071-0.

The advantages of microbore columns for trace analysis by liquid chromatography are identified, with reference to on-column enrichment techniques performed on analytical micro-columns. The selectivity and high sensitivity of the amperometric detector are utilized in combination with a microbore...

Cite
Krejci M, Slais K, Kourilová D, et al. Enrichment techniques and trace analysis with microbore columns in liquid chromatography. J Pharm Biomed Anal. 1984;2(2):197-205doi: 10.1016/0731-7085(84)80071-0.
Krejci, M., Slais, K., Kourilová, D., & Vespalcová, M. (1984). Enrichment techniques and trace analysis with microbore columns in liquid chromatography. Journal of pharmaceutical and biomedical analysis, 2(2), 197-205. https://doi.org/10.1016/0731-7085(84)80071-0
Krejci, M, et al. "Enrichment techniques and trace analysis with microbore columns in liquid chromatography." Journal of pharmaceutical and biomedical analysis vol. 2,2 (1984): 197-205. doi: https://doi.org/10.1016/0731-7085(84)80071-0
Krejci M, Slais K, Kourilová D, Vespalcová M. Enrichment techniques and trace analysis with microbore columns in liquid chromatography. J Pharm Biomed Anal. 1984;2(2):197-205. doi: 10.1016/0731-7085(84)80071-0. PMID: 16867748.
Copy Download .nbib Format: NLM
Showing 13 to 24 of 476 entries